RPOC_AQUPY
ID RPOC_AQUPY Reviewed; 1576 AA.
AC Q9X6Y2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322};
OS Aquifex pyrophilus.
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=2714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX PubMed=10198119; DOI=10.1007/pl00006496;
RA Klenk H.-P., Meier T.D., Durovic P., Schwass V., Lottspeich F.,
RA Dennis P.P., Zillig W.;
RT "RNA polymerase of Aquifex pyrophilus: implications for the evolution of
RT the bacterial rpoBC operon and extremely thermophilic bacteria.";
RL J. Mol. Evol. 48:528-541(1999).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; X75046; CAA52958.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X6Y2; -.
DR SMR; Q9X6Y2; -.
DR PRIDE; Q9X6Y2; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1576
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067702"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 594
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1002
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1576 AA; 178432 MW; 332A117F1EB39A9B CRC64;
MSTKGRGIFP FSKIKLMLAS PDDIRSWSHG EVKRPETLNY RTLKPEKDGL FCAKIFGPTK
DYECLCGKYR GKRYEGKICE KCGVEVTSSY VRRERFGHIE LAAPVVHIWF LKSTPSKIGT
LLNLTSRDVE RVAYFESYLV IEYPNEEEEE KFEKEEGTIP LNDGISTKWV KLHVVNEEEF
EEKYAFSIDE KYEYGMGAEI LKEVLSKIDL EAYSKKLKEL VKPYSLGFED LGREVAEKYK
NLYQKLVKVI ADDFRAYGVE LKGLEDKGLT LEQAIHRIIT EELYLNVETG EVEFEDCGDN
CLTGREALRV YYEKVREHKR DIPIFEKIKE DVRTAVLREV SEARIRKALR ILQLVEGFKK
SGNRPEWMIL EVLPVIPPEL RPLVALDGGR FATSDLNDLY RRVINRNNRL KRLIELSAPD
IIIRNEKRML QEAVDALIDN GKRGNPVKQN GRPLKSLADY LKGKQGRFRQ NLLGKRVDYS
GRSVIVVGPE LQMHQCGLPK IMALELFKPF VYRRLEEKGY ATSIKHAKKL VEQKTPEVWE
CLEEVVKQHP VLLNRAPTLH RPSIQAFEPV LVEGKAIQLH PLVCPPFNAD FDGDQMAVHV
PLGIEAQLES YILMLSTQNI LSPAHGKPLT MPSQDMVLGT YYMTHDPIPG RKGEGKAFTS
YEEVIKALEL GHVDIHAKIK FKVGKEWIET TPGRVLFNSI MPEGQPFVNE TLDKKRLSKL
ITNLYIAVGN EETVKFLDRV KELGFLRSTL AGISIGIDDL QVPKVKEKII KEALKKTEEI
WNQYVQGIIT NKERYNRIID VWSEATNAVS KAMFEEIEHS TEIRNGKEYP GTFNPIYMMA
VSGARGNRDQ IRQLAGMRGL MAKHSGEFIE TPIISNFREG LSVLEYFIST YGARKGLADT
ALKTAFAGYL TRRLVDVAQD ITITEKDCGT VKGFEMEPIV EAGEERVPLK DRIFGRVLAE
DVKDPYTGEV IAKRNEVVDE KLAERIARAG IEKVKVRSPL TCEAKHGVCA MCYGWDLSQR
KIVSVGEAVG IIAAQSIGEP GTQLTMRTFH IGGAATAQKV QSFVKTESEG TVKFYNVKFI
VNRKGEKINV SKDAAIGVLD EKGRLLERHT IPYGARLLVD EGQKVKAGTK LADWDPFNTY
IIAEVGGKIE LRDIILDVTV REERDVITGK TATVVSFMRP KDAMLHTPRI AVITEDGKEY
VYDLPVNAIL NIPADKLTLE WRICPTCSES EETTIQHQYY VVKELEVQPG DILARIPKET
AKVRDIVGGL PRVEELFEAR KPKNPAILSE IDGYVKIYED ADEVIVFNPR TGETKKYAIK
KDELILVRHG QYIKKGQKIT ETKVAEIDGQ VRIKGRGFKV IVYNPETGLQ REYFVPKGKF
LLVKEGDYVK AGDPLTDGTP VPEEILRIKG IEELEKFLLK EVQMVYKLQG VDINDKHFEI
IIRQMLKKVR IIDPGDSRFL VGEEVDKEEL EEEIQRIKLE GGKLPKAEPV LVGITRAALS
TRSWISAASF QETTRVLTDA SVEGKIDELR GLKENVIIGN LIPAGTGVDE YKEVDVIPAE
EKVLEEKPQS SEEETS
